ID   PPA28_ARATH             Reviewed;         397 AA.
AC   Q9LU72;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Probable inactive purple acid phosphatase 28;
DE   Flags: Precursor;
GN   Name=PAP28; OrderedLocusNames=At5g57140; ORFNames=MUL3.9;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia;
RX   PubMed=16244908; DOI=10.1007/s11103-005-0183-0;
RA   Zhu H., Qian W., Lu X., Li D., Liu X., Liu K., Wang D.;
RT   "Expression patterns of purple acid phosphatase genes in Arabidopsis organs
RT   and functional analysis of AtPAP23 predominantly transcribed in flower.";
RL   Plant Mol. Biol. 59:581-594(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT   features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:31-63(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=12021284; DOI=10.1074/jbc.m204183200;
RA   Li D., Zhu H., Liu K., Liu X., Leggewie G., Udvardi M., Wang D.;
RT   "Purple acid phosphatases of Arabidopsis thaliana. Comparative analysis and
RT   differential regulation by phosphate deprivation.";
RL   J. Biol. Chem. 277:27772-27781(2002).
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC       Note=Binds 1 Fe cation per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, flowers and
CC       siliques. {ECO:0000269|PubMed:16244908}.
CC   -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. Purple
CC       acid phosphatase family. {ECO:0000305}.
CC   -!- CAUTION: Lacks the conserved His residue essential for phosphatase
CC       activity. Its enzyme activity is therefore unsure. {ECO:0000305}.
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DR   EMBL; AY882860; AAW80660.1; -; mRNA.
DR   EMBL; AB023042; BAA97364.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED96852.1; -; Genomic_DNA.
DR   EMBL; AY136380; AAM97046.1; -; mRNA.
DR   EMBL; BT002110; AAN72121.1; -; mRNA.
DR   RefSeq; NP_200524.1; NM_125096.3.
DR   AlphaFoldDB; Q9LU72; -.
DR   STRING; 3702.AT5G57140.1; -.
DR   PaxDb; Q9LU72; -.
DR   PRIDE; Q9LU72; -.
DR   ProteomicsDB; 249029; -.
DR   EnsemblPlants; AT5G57140.1; AT5G57140.1; AT5G57140.
DR   GeneID; 835820; -.
DR   Gramene; AT5G57140.1; AT5G57140.1; AT5G57140.
DR   KEGG; ath:AT5G57140; -.
DR   Araport; AT5G57140; -.
DR   TAIR; locus:2175594; AT5G57140.
DR   eggNOG; KOG1432; Eukaryota.
DR   HOGENOM; CLU_019692_0_0_1; -.
DR   InParanoid; Q9LU72; -.
DR   OMA; PNWHRRA; -.
DR   OrthoDB; 908967at2759; -.
DR   PhylomeDB; Q9LU72; -.
DR   PRO; PR:Q9LU72; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9LU72; baseline and differential.
DR   Genevisible; Q9LU72; AT.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0003993; F:acid phosphatase activity; ISS:TAIR.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR011230; Pesterase_At2g46.
DR   Pfam; PF00149; Metallophos; 1.
DR   PIRSF; PIRSF030250; Ptase_At2g46880; 1.
DR   SUPFAM; SSF56300; SSF56300; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Iron; Metal-binding; Reference proteome; Secreted; Signal;
KW   Zinc.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..397
FT                   /note="Probable inactive purple acid phosphatase 28"
FT                   /id="PRO_0000372830"
FT   BINDING         266
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         314..316
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         314
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         316
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        91
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        209
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   397 AA;  45437 MW;  ED5DBE0208E91981 CRC64;
     MNCSIGNWKH TVLYLTLIVS LLYFIESLIS HKLHINYNKI RLKRSPNLPL RFRDDGTFKI
     LQVADMHFGM GMITRCRDVL DSEFEYCSDL NTTRFLRRMI ESERPDLIAF TGDNIFGSST
     TDAAESLLEA IGPAIEYGIP WAAVLGNHDH ESTLNRLELM TFLSLMDFSV SQINPLVEDE
     TKGDTMRLID GFGNYRVRVY GAPGSVLANS TVFDLFFFDS GDREIVQGKR TYGWIKESQL
     RWLQDTSIQG HSQRIHVNPP ALAFFHIPIL EVRELWYTPF IGQFQEGVAC SIVQSGVLQT
     FVSMGNVKAA FMGHDHVNDF CGTLKGVWFC YGGGFGYHAY GRPNWHRRAR VIEAKLGKGR
     DTWEGIKLIK TWKRLDDEYL SKIDEQVLWE TSDSFLK